Cooperative Regulation of <i>DOG2</i> , Encoding 2-Deoxyglucose-6-Phosphate Phosphatase, by Snf1 Kinase and the High-Osmolarity Glycerol–Mitogen-Activated Protein Kinase Cascade in Stress Responses of <i>Saccharomyces cerevisiae</i>

<jats:title>ABSTRACT</jats:title> <jats:p> We screened the genome of <jats:italic>Saccharomyces cerevisiae</jats:italic> for the genes responsive to oxidative stress by using the <jats:italic>lacZ</jats:italic> transposon-insertion library. As a result, we found that expression of the <jats:italic>DOG2</jats:italic> gene coding for 2-deoxyglucose-6-phosphate phosphatase was induced by oxidative stress. The expression of <jats:italic>DOG2</jats:italic> was also induced by osmotic stress. We found a putative <jats:italic>cis</jats:italic> element (STRE, a stress response element) in the <jats:italic>DOG2</jats:italic> promoter adjacent to a consensus sequence to which the Mig1p repressor is known to bind. The basal levels of <jats:italic>DOG2</jats:italic> gene expression were increased in a <jats:italic>mig1</jats:italic> Δ mutant, while the derepression of <jats:italic>DOG2</jats:italic> was not observed in a <jats:italic>snf1</jats:italic> Δ mutant under glucose-deprived conditions. Induction of the <jats:italic>DOG2</jats:italic> gene expression by osmotic stress was observed in any of the three disruptants <jats:italic>pbs2</jats:italic> Δ, <jats:italic>hog1</jats:italic> Δ, and <jats:italic>snf1</jats:italic> Δ. However, the osmotic induction was completely abolished in both the <jats:italic>snf1Δ pbs2</jats:italic> Δ mutant and the <jats:italic>snf1Δ hog1</jats:italic> Δ mutant. Additionally, these single mutants as well as double mutants failed to induce <jats:italic>DOG2</jats:italic> expression by oxidative stress. These results suggest that Snf1p kinase and the high-osmolarity glycerol–mitogen-activated protein kinase cascade are likely to be involved in the signaling pathway of oxidative stress and osmotic stress in regulation of <jats:italic>DOG2</jats:italic> . </jats:p>